Year |
Citation |
Score |
2010 |
Seetharaman SV, Winkler DD, Taylor AB, Cao X, Whitson LJ, Doucette PA, Valentine JS, Schirf V, Demeler B, Carroll MC, Culotta VC, Hart PJ. Disrupted zinc-binding sites in structures of pathogenic SOD1 variants D124V and H80R. Biochemistry. 49: 5714-25. PMID 20515040 DOI: 10.1021/Bi100314N |
0.706 |
|
2009 |
Oztug Durer ZA, Cohlberg JA, Dinh P, Padua S, Ehrenclou K, Downes S, Tan JK, Nakano Y, Bowman CJ, Hoskins JL, Kwon C, Mason AZ, Rodriguez JA, Doucette PA, Shaw BF, et al. Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase. Plos One. 4: e5004. PMID 19325915 DOI: 10.1371/Journal.Pone.0005004 |
0.751 |
|
2008 |
Cao X, Antonyuk SV, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, Hart PJ. Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis. The Journal of Biological Chemistry. 283: 16169-77. PMID 18378676 DOI: 10.1074/Jbc.M801522200 |
0.672 |
|
2007 |
Potter SZ, Zhu H, Shaw BF, Rodriguez JA, Doucette PA, Sohn SH, Durazo A, Faull KF, Gralla EB, Nersissian AM, Valentine JS. Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein. Journal of the American Chemical Society. 129: 4575-83. PMID 17381088 DOI: 10.1021/Ja066690+ |
0.568 |
|
2006 |
Strange RW, Antonyuk SV, Hough MA, Doucette PA, Valentine JS, Hasnain SS. Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymes. Journal of Molecular Biology. 356: 1152-62. PMID 16406071 DOI: 10.1016/J.Jmb.2005.11.081 |
0.639 |
|
2005 |
Rodriguez JA, Shaw BF, Durazo A, Sohn SH, Doucette PA, Nersissian AM, Faull KF, Eggers DK, Tiwari A, Hayward LJ, Valentine JS. Destabilization of apoprotein is insufficient to explain Cu,Zn-superoxide dismutase-linked ALS pathogenesis. Proceedings of the National Academy of Sciences of the United States of America. 102: 10516-21. PMID 16020530 DOI: 10.1073/Pnas.0502515102 |
0.726 |
|
2005 |
Valentine JS, Doucette PA, Zittin Potter S. Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annual Review of Biochemistry. 74: 563-93. PMID 15952898 DOI: 10.1146/Annurev.Biochem.72.121801.161647 |
0.632 |
|
2005 |
Antonyuk S, Elam JS, Hough MA, Strange RW, Doucette PA, Rodriguez JA, Hayward LJ, Valentine JS, Hart PJ, Hasnain SS. Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46Arg. Protein Science : a Publication of the Protein Society. 14: 1201-13. PMID 15840828 DOI: 10.1110/Ps.041256705 |
0.743 |
|
2004 |
Doucette PA, Whitson LJ, Cao X, Schirf V, Demeler B, Valentine JS, Hansen JC, Hart PJ. Dissociation of human copper-zinc superoxide dismutase dimers using chaotrope and reductant. Insights into the molecular basis for dimer stability. The Journal of Biological Chemistry. 279: 54558-66. PMID 15485869 DOI: 10.1074/Jbc.M409744200 |
0.659 |
|
2004 |
Hough MA, Grossmann JG, Antonyuk SV, Strange RW, Doucette PA, Rodriguez JA, Whitson LJ, Hart PJ, Hayward LJ, Valentine JS, Hasnain SS. Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutants. Proceedings of the National Academy of Sciences of the United States of America. 101: 5976-81. PMID 15056757 DOI: 10.1073/Pnas.0305143101 |
0.689 |
|
2003 |
Elam JS, Taylor AB, Strange R, Antonyuk S, Doucette PA, Rodriguez JA, Hasnain SS, Hayward LJ, Valentine JS, Yeates TO, Hart PJ. Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Nature Structural Biology. 10: 461-7. PMID 12754496 DOI: 10.1038/Nsb935 |
0.711 |
|
2003 |
Strange RW, Antonyuk S, Hough MA, Doucette PA, Rodriguez JA, Hart PJ, Hayward LJ, Valentine JS, Hasnain SS. The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis. Journal of Molecular Biology. 328: 877-91. PMID 12729761 DOI: 10.1016/S0022-2836(03)00355-3 |
0.76 |
|
2003 |
Elam JS, Malek K, Rodriguez JA, Doucette PA, Taylor AB, Hayward LJ, Cabelli DE, Valentine JS, Hart PJ. An alternative mechanism of bicarbonate-mediated peroxidation by copper-zinc superoxide dismutase: rates enhanced via proposed enzyme-associated peroxycarbonate intermediate. The Journal of Biological Chemistry. 278: 21032-9. PMID 12649272 DOI: 10.1074/Jbc.M300484200 |
0.65 |
|
2003 |
Hart P, Elam JS, Taylor AB, Strange R, Hasnain S, Doucette PA, Valentine JS, Hayward LJ. Misfolded superoxide dismutase and ALS Journal of Inorganic Biochemistry. 96: 44. DOI: 10.1016/S0162-0134(03)80479-8 |
0.437 |
|
2002 |
Antonyuk SV, Hough MA, Strange RW, Doucette P, Hart PJ, Valentine JS, Hasnain SS. High resolution structures of wild type and apo human CuZn superoxide dismutase and its fals-related mutants Acta Crystallographica Section a Foundations of Crystallography. 58: c116-c116. DOI: 10.1107/S0108767302089687 |
0.513 |
|
2002 |
Elam JS, Malek K, Rodriguez JA, Doucette PA, Taylor AB, Hayward LJ, Cabelli DE, Valentine JS, Hart PJ, Jankova L. Structure of FALS mutant CuZnSOD D125H: implications bicarbonate's role in peroxidative reactions catalyzed by CuZnSOD Acta Crystallographica Section a Foundations of Crystallography. 58: c91-c91. DOI: 10.1107/S0108767302088657 |
0.63 |
|
Show low-probability matches. |